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Chlorophyllase type 0 (EC 3.1.1.14) (CaCLH0) (Chlorophyll-chlorophyllido hydrolase 0) (Chlase 0)

 CLH0_CHEAL              Reviewed;         347 AA.
Q9LE89;
16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
05-DEC-2018, entry version 78.
RecName: Full=Chlorophyllase type 0;
EC=3.1.1.14;
AltName: Full=CaCLH0;
AltName: Full=Chlorophyll-chlorophyllido hydrolase 0;
Short=Chlase 0;
Flags: Precursor;
Name=CACLH;
Chenopodium album (Fat-hen).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; Caryophyllales; Chenopodiaceae; Chenopodioideae;
Atripliceae; Chenopodium.
NCBI_TaxID=3559;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 34-51; 156-166 AND
250-256.
TISSUE=Leaf;
PubMed=10611389; DOI=10.1073/pnas.96.26.15362;
Tsuchiya T., Ohta H., Okawa K., Iwamatsu A., Shimada H., Masuda T.,
Takamiya K.;
"Cloning of chlorophyllase, the key enzyme in chlorophyll degradation:
finding of a lipase motif and the induction by methyl jasmonate.";
Proc. Natl. Acad. Sci. U.S.A. 96:15362-15367(1999).
[2]
INHIBITION, AND MUTAGENESIS OF HIS-81; HIS-100; HIS-161; SER-162;
SER-167; ASP-191; CYS-234; HIS-241; CYS-248; HIS-254; HIS-262; ASP-264
AND CYS-282.
PubMed=12552153; DOI=10.1093/pcp/pcg011;
Tsuchiya T., Suzuki T., Yamada T., Shimada H., Masuda T., Ohta H.,
Takamiya K.;
"Chlorophyllase as a serine hydrolase: identification of a putative
catalytic triad.";
Plant Cell Physiol. 44:96-101(2003).
-!- FUNCTION: Catalyzes the hydrolysis of ester bond in chlorophyll to
yield chlorophyllide and phytol.
-!- CATALYTIC ACTIVITY:
Reaction=a chlorophyll + H2O = a chlorophyllide + H(+) + phytol;
Xref=Rhea:RHEA:19605, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:17327, ChEBI:CHEBI:139291, ChEBI:CHEBI:139292;
EC=3.1.1.14;
-!- ACTIVITY REGULATION: Inhibited by diisopropyl fluorophosphate
(DFP), phenylmethanesulfonyl fluoride (PMSF) or p-
chloromercuribenzoic acid (PCMB), but not by N-ethylmaleimide
(NEM) or iodoacetamide.
-!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
degradation.
-!- MISCELLANEOUS: It has been proposed that CaCLH0 is transported to
vacuole via the endoplasmic reticulum where it might be
glycosylated.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
family. {ECO:0000305}.
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EMBL; AB025025; BAA93635.1; -; mRNA.
EMBL; AF134301; AAF27045.1; -; mRNA.
ProteinModelPortal; Q9LE89; -.
SwissLipids; SLP:000001500; -.
ESTHER; cheal-CACLH; Chlorophyllase.
KEGG; ag:AAF27045; -.
KO; K08099; -.
BRENDA; 3.1.1.14; 1304.
UniPathway; UPA00674; -.
GO; GO:0047746; F:chlorophyllase activity; IEA:UniProtKB-EC.
GO; GO:0102293; F:pheophytinase b activity; IEA:UniProtKB-EC.
GO; GO:0015996; P:chlorophyll catabolic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR017395; Chlorophyllase.
Pfam; PF07224; Chlorophyllase; 1.
PIRSF; PIRSF038128; Chlorophyllase_chloroplast; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00120; LIPASE_SER; 1.
1: Evidence at protein level;
Chlorophyll catabolism; Direct protein sequencing; Glycoprotein;
Hydrolase; Signal.
SIGNAL 1 19 {ECO:0000255}.
PROPEP 20 30 {ECO:0000250}.
/FTId=PRO_0000017837.
CHAIN 31 347 Chlorophyllase type 0.
/FTId=PRO_0000017838.
ACT_SITE 162 162 Nucleophile.
ACT_SITE 191 191 Charge relay system.
ACT_SITE 262 262 Charge relay system.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 251 251 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 321 321 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 81 81 H->A: Reduction of activity.
{ECO:0000269|PubMed:12552153}.
MUTAGEN 100 100 H->A: Severe loss of activity.
{ECO:0000269|PubMed:12552153}.
MUTAGEN 161 161 H->A: Total loss of activity.
{ECO:0000269|PubMed:12552153}.
MUTAGEN 162 162 S->A: Total loss of activity.
{ECO:0000269|PubMed:12552153}.
MUTAGEN 167 167 S->A: Slight reduction of activity.
{ECO:0000269|PubMed:12552153}.
MUTAGEN 191 191 D->N: Total loss of activity.
{ECO:0000269|PubMed:12552153}.
MUTAGEN 234 234 C->A: Severe loss of activity.
{ECO:0000269|PubMed:12552153}.
MUTAGEN 241 241 H->A: Reduction of activity.
{ECO:0000269|PubMed:12552153}.
MUTAGEN 248 248 C->A: Reduction of activity.
{ECO:0000269|PubMed:12552153}.
MUTAGEN 254 254 H->A: Total loss of activity.
{ECO:0000269|PubMed:12552153}.
MUTAGEN 254 254 H->Y: Reduction of activity.
{ECO:0000269|PubMed:12552153}.
MUTAGEN 262 262 H->A,Y: Total loss of activity.
{ECO:0000269|PubMed:12552153}.
MUTAGEN 264 264 D->N: Severe loss of activity.
{ECO:0000269|PubMed:12552153}.
MUTAGEN 282 282 C->A: Severe loss of activity.
{ECO:0000269|PubMed:12552153}.
SEQUENCE 347 AA; 38707 MW; 03EB2C5B8259B863 CRC64;
MAKLLLLIFG VFIFVNSQAQ TFPTILEKHN SEKITDVFHK GNFQVTNNPI RVKRYEFSAP
EPLIIISPKE AGVYPVLLFI HGTMLSNEDY SLFFNYIASH GFIVVAPKLF RLFPPKLPSQ
QDEIDMAASV ANWMPLYLQV VLQRYVTGVE GDLEKLAISG HSRGGKSAFA LALGFSNIKL
DVTFSALIGV DPVAGRSVDD RTLPHVLTYK PNSFNLSIPV TVIGSGLGNH TISCAPNHVS
HQQFYDECKE NSSHFVITKY GHMDMLNEFR LSPIAVTMSL MCAQSFRPKA TMRRTLGGIM
VAFLNAYFRD DGRQYYAIIA NRSLAPTNLF AEKKGFNFGF ATTYAQL


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